ArticleNature microbiology2024
Secretion of the fungal toxin candidalysin is dependent on conserved precursor peptide sequences.
Article in Nature microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The trial behind it
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Who cites it
14 citing papers in PubMed, 15 citations in OpenAlex.
- Peptide YY reduces cytotoxicity of Candida albicans in alcohol-associated liver disease.JHEP reports : innovation in hepatology · 2026Article
- Candidalysin at the epithelial-systemic interface: mechanistic evidence, critical-care relevance, and translational opportunities in invasive candidiasis.Frontiers in cellular and infection microbiology · 2026Review
- Tight junction suppression by candidalysin promotes gut-to-blood dissemination ofFrontiers in microbiology · 2026Article
- Review
- The fungal peptide toxin candidalysin induces distinct membrane repair mechanisms compared to bacterial pore-forming toxins.Cell death discovery · 2025Article
- Dynamic expression of candidalysin facilitates oral colonization of Candida albicans in mice.Nature microbiology · 2025Article
- "Pour some sugar on me"-Environmental Candida albicans isolates and the evolution of increased pathogenicity and antifungal resistance through sugar adaptation.PLoS pathogens · 2025Article
- Insights into the evolution of Candidalysin and recent developments.Archives of microbiology · 2025Review
- Review
- Host targets of candidalysin.PLoS pathogens · 2025Review
- Article
- Vaginal Candida albicans infections: host-pathogen-microbiome interactions.FEMS microbiology reviews · 2025Review
- An approach to analyze spatiotemporal patterns of gene expression at single-cell resolution inmSphere · 2024Article
- Article
Corrections and comments
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Authors and funding
27 authors at 7 institutions in 4 countries.
Funding
Abstract
The opportunistic fungal pathogen Candida albicans damages host cells via its peptide toxin, candidalysin. Before secretion, candidalysin is embedded in a precursor protein, Ece1, which consists of a signal peptide, the precursor of candidalysin and seven non-candidalysin Ece1 peptides (NCEPs), and is found to be conserved in clinical isolates. Here we show that the Ece1 polyprotein does not resemble the usual precursor structure of peptide toxins. C. albicans cells are not susceptible to their own toxin, and single NCEPs adjacent to candidalysin are sufficient to prevent host cell toxicity. Using a series of Ece1 mutants, mass spectrometry and anti-candidalysin nanobodies, we show that NCEPs play a role in intracellular Ece1 folding and candidalysin secretion. Removal of single NCEPs or modifications of peptide sequences cause an unfolded protein response (UPR), which in turn inhibits hypha formation and pathogenicity in vitro. Our data indicate that the Ece1 precursor is not required to block premature pore-forming toxicity, but rather to prevent intracellular auto-aggregation of candidalysin sequences.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.